PcrB

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  • Description: heptaprenylglyceryl phosphate synthase

Gene name pcrB
Synonyms yerE
Essential no
Product heptaprenylglyceryl phosphate synthase
Function unknown
Gene expression levels in SubtiExpress: pcrB
MW, pI 24 kDa, 4.204
Gene length, protein length 684 bp, 228 aa
Immediate neighbours yerD, pcrA
Sequences Protein DNA DNA_with_flanks
Genetic context
PcrB context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
PcrB expression.png
























Categories containing this gene/protein

lipid metabolism/ other

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU06600

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
    • production of heptaprenylglyceryl phosphate from heptaprenyl diphosphate and glycerol-1-phosphate PubMed
  • Protein family: GGGP synthase family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Sigma factor:
  • Regulation:
  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Feifei Ren, Xinxin Feng, Tzu-Ping Ko, Chun-Hsiang Huang, Yumei Hu, Hsiu-Chien Chan, Yi-Liang Liu, Ke Wang, Chun-Chi Chen, Xuefei Pang, Miao He, Yujie Li, Eric Oldfield, Rey-Ting Guo
Insights into TIM-barrel prenyl transferase mechanisms: crystal structures of PcrB from Bacillus subtilis and Staphylococcus aureus.
Chembiochem: 2013, 14(2);195-9
[PubMed:23322418] [WorldCat.org] [DOI] (I p)

David Peterhoff, Hermann Zellner, Harald Guldan, Rainer Merkl, Reinhard Sterner, Patrick Babinger
Dimerization determines substrate specificity of a bacterial prenyltransferase.
Chembiochem: 2012, 13(9);1297-303
[PubMed:22614947] [WorldCat.org] [DOI] (I p)

Harald Guldan, Frank-Michael Matysik, Marco Bocola, Reinhard Sterner, Patrick Babinger
Functional assignment of an enzyme that catalyzes the synthesis of an archaea-type ether lipid in bacteria.
Angew Chem Int Ed Engl: 2011, 50(35);8188-91
[PubMed:21761520] [WorldCat.org] [DOI] (I p)

Harald Guldan, Reinhard Sterner, Patrick Babinger
Identification and characterization of a bacterial glycerol-1-phosphate dehydrogenase: Ni(2+)-dependent AraM from Bacillus subtilis.
Biochemistry: 2008, 47(28);7376-84
[PubMed:18558723] [WorldCat.org] [DOI] (I p)

M A Petit, E Dervyn, M Rose, K D Entian, S McGovern, S D Ehrlich, C Bruand
PcrA is an essential DNA helicase of Bacillus subtilis fulfilling functions both in repair and rolling-circle replication.
Mol Microbiol: 1998, 29(1);261-73
[PubMed:9701819] [WorldCat.org] [DOI] (P p)